STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
EDS75105.1KEGG: ctc:CTC01806 2.7e-209 5-methyltetrahydrofolate--homocysteine methyltransferase K00548; COG: COG1410 Methionine synthase I, cobalamin-binding domain; Psort location: Cytoplasmic, score: 8.87. (785 aa)    
Predicted Functional Partners:
metF
KEGG: mxa:MXAN_3039 1.4e-61 metF; 5,10-methylenetetrahydrofolate reductase; COG: COG0685 5,10-methylenetetrahydrofolate reductase; Psort location: Cytoplasmic, score: 8.87.
 
 
 0.999
EDS75104.1
Vitamin B12 dependent methionine synthase, activation domain protein; KEGG: ctc:CTC01807 5.9e-24 putative 5-methyltetrahydrofolate--homocysteine methyltransferase K00548; COG: NOG21937 non supervised orthologous group; Psort location: Cytoplasmic, score: 8.87.
 
  
 0.969
metK
Methionine adenosyltransferase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
  
 
 0.957
EDS74130.1
O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase; KEGG: gka:GK0284 6.0e-118 O-acetylhomoserine sulfhydrylase K01740; COG: COG2873 O-acetylhomoserine sulfhydrylase; Psort location: Cytoplasmic, score: 9.98.
  
 
 0.957
luxS
S-ribosylhomocysteinase LuxS; Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). Belongs to the LuxS family.
    
 0.956
fhs
KEGG: mta:Moth_0109 5.8e-207 formate--tetrahydrofolate ligase K01938; COG: COG2759 Formyltetrahydrofolate synthetase; Psort location: Cytoplasmic, score: 8.87.
  
 
 0.956
glyA
Glycine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
   
 
 0.942
hly
Hemolysin; KEGG: tde:TDE2410 4.8e-100 hemolysin K00842; COG: COG1168 Bifunctional PLP-dependent enzyme with beta-cystathionase and maltose regulon repressor activities; Psort location: Cytoplasmic, score: 8.87.
     
 0.940
EDS75697.1
KEGG: aae:aq_1812 4.4e-67 thrA; homoserine dehydrogenase K00003; COG: COG0460 Homoserine dehydrogenase; Psort location: Cytoplasmic, score: 8.87.
  
 
 0.939
ilvA
Threonine ammonia-lyase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
  
 0.931
Your Current Organism:
Clostridium spiroforme
NCBI taxonomy Id: 428126
Other names: Clostridium spiroforme ATCC 29900, [. spiroforme DSM 1552, [Clostridium] spiroforme DSM 1552
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